1,4-Butanediol diglycidyl ether coupling of carbohydrates to sepharose: Affinity adsorbents for lectins and glycosidases

Uy, Rosa; Wold, Finn

doi:10.1016/0003-2697(77)90602-9

Cited by 67 publications

(16 citation statements)

References 15 publications

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“…6 A and B, which is published as supporting information on the PNAS web site). A control solution, largely depleted of SP-A, was prepared by passing the SP-A-enriched preparation over a D-Mannose column (Sigma) (29). The SP-A-depleted preparation was examined for remaining SP-A content by immunoblot analysis (Fig.…”

Section: Methodsmentioning

confidence: 99%

Surfactant protein secreted by the maturing mouse fetal lung acts as a hormone that signals the initiation of parturition

Condon

Jeyasuria

Faust

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

324

277

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Section: Methodsmentioning

confidence: 99%

Surfactant protein secreted by the maturing mouse fetal lung acts as a hormone that signals the initiation of parturition

Condon

Jeyasuria

Faust

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

324

277

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“…PNA was isolated from raw peanuts (kindly donated by Astra, Steffisburg, Switzerland) by affinity chromatography of a crude saline extract (15) on lactose coupled to Sepharose (16) and was coupled to polyacrylic hydrazide-Sepharose by the method of Wilchek and Miron (17) at 1.7 mg/ml.…”

Section: Materiais and Methodsmentioning

confidence: 99%

Relationship between glycocalicin and glycoprotein Ib of human platelets.

Clemetson¹,

Naim²,

Lüscher³

1981

Proc. Natl. Acad. Sci. U.S.A.

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Asialoglycoprotein lb and asialoglycocalicin have been isolated from the membranes and from the supernatant, respectively, after sonication of neuraminidase-treated platelets, by lectin affinity chromatography on peanut agglutinin. The isolated asialoglycoprotein lb had an apparent molecular weight of 160,000 when not reduced and 150,000 when reduced, whereas the asialoglycocalicin had an apparent molecular weight of 150,000, both reduced and unreduced, on sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Both preparations contained only trace amounts of impurities. The asialoglycoprotein lb and asialoglycocalicin in both the unreduced and reduced states were separated by gel electrophoresis, radioiodinated in gel slices, and digested with trypsin, and the digests were analyzed by two-dimensional high-voltage electrophoresis and thin-layer chromatography followed by autoradiography. The tryptic peptide maps showed great similarities between glycocalicin and glycoprotein lb, with the latter (both unreduced and reduced) containing additional peptides, supporting the idea that glycocalicin is derived from glycoprotein lb. The unreduced glycoprotein Ib contained additional peptides compared to the reduced due to the disulfide-bond-linked (3com-ponent. There were also slight differences between unreduced and reduced glycocalicin, indicating that at least one intramolecular disulfide bond is present.

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“…The conditions known to lead to a high substitution of Sepharose by epoxides [25] gave in the present case products which contained only 5 % of covalently bound Triton X-100 residues. Dextran is a polysaccharide which contains only secondary hydroxyls; since the reaction of epoxides with primary hydroxyls is known to proceed faster than with the secondary one [26], the same procedure was applied to polysaccharides containing primary hydroxyls. Cellulose and amylose gave products 8(5 %) and 7(19%).…”

Section: Preparation Of Polysaccharide Derivativesmentioning

confidence: 99%

Detergents Linked to Polysaccharides: Preparation and Effects on Membranes and Cells

Pitha

Kociolek

Caron

1979

European Journal of Biochemistry

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Residues of Triton X-100 [ C~H I~-C~H~-( O -C H~-C H~)~-10-0-1 were bound by ether bonds to inulin, dextran, amylose, and cellulose-yielding compounds containing 10-30, 5, 19 and 6 % (w/w)of Triton X-100 residue respectively. The water-soluble inulin derivative was studied in detail. This compound was fractionated on the basis of molecular weight by gel chromatography and on the basis of degree of substitution by adsorption to polystyrene resin. Even the residues of Triton X-100 which were bound to a single inulin macromolecule were able to form a micelle; in addition to these monomolecular micelles the inulin derivative was able to form polymolecular micelles as well. The inulin derivative was effective in solubilizing proteins and phospholipids from membranes of human erythrocytes and liberated reverse transcriptase activity from the membrane-enveloped virions of murine leukemia. The Triton X-100 inulin derivative abolished binding of the 3H-labelled antagonist dihydroalprenolol to solubilized preparations of P-adrenergic receptors from frog erythrocytes in a dose-related manner similar to the inactivation produced by Triton X-100, while digitonin, a detergent containing a bulkier hydrophobic group, did not cause inactivation. On the basis of its Triton X-100 content, the inulin derivative was found to be less detrimental to the growth of murine erythroleukemic cells in vitro than Triton X-100 alone when short (2-4 h) exposures were used, but this difference disappeared at longer (1 -3 day) exposures. Results thus suggest that the increase in size of the hydrophilic part of the detergent brings about moderation in those effects of the detergent which are dependent on the rate of diffusion, while the solubilizing and inactivating effects of the detergent were not changed. It is probably the size of the hydrophobic part which is important in protein-inactivating properties of the detergent.Biochemical studies of membrane components and studies of metabolism of permeabilized cells rely on the use of detergents [l]. Industrial detergents have found wide-spread use in the disruption and solubilization of biological structures. However, in applications where very mild action is desired suitable detergents are still not available. If the retention of biological activity is desired in the solubilized membrane preparations, only a few detergent molecules should be bound to a protein in order to minimize any alteration of its structure. Nevertheless even the mild electroneutral detergent Triton X-100 replaces all the natural lipids in lipoproteins and is massively bound to lipophilic proteins [2 -4,7]. Even in these unphysiological conditions some proteins continue to function [5 -71, while in other proteins, biological activities are lost [l]. In making cells permeable, similar detergents not only dissolve the plasma membrane but also penetrate and diffuse into the interior of the cells [8 -111. We reasoned that certain improvement in all of these applications may be achieved by using detergents which would have bulky ...

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1,4-Butanediol diglycidyl ether coupling of carbohydrates to sepharose: Affinity adsorbents for lectins and glycosidases

Cited by 67 publications

References 15 publications

Surfactant protein secreted by the maturing mouse fetal lung acts as a hormone that signals the initiation of parturition

Surfactant protein secreted by the maturing mouse fetal lung acts as a hormone that signals the initiation of parturition

Relationship between glycocalicin and glycoprotein Ib of human platelets.

Detergents Linked to Polysaccharides: Preparation and Effects on Membranes and Cells

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